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Database: UniProt
Entry: A0A3B6ELV8_WHEAT
LinkDB: A0A3B6ELV8_WHEAT
Original site: A0A3B6ELV8_WHEAT 
ID   A0A3B6ELV8_WHEAT        Unreviewed;       851 AA.
AC   A0A3B6ELV8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF7024501.1, ECO:0000313|EnsemblPlants:TraesCS3A02G354200.2};
GN   ORFNames=CFC21_036839 {ECO:0000313|EMBL:KAF7024501.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3A02G354200.2};
RN   [1] {ECO:0000313|EMBL:KAF7024501.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7024501.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS3A02G354200.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS3A02G354200.2};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS3A02G354200.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7024501.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7024501.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC       {ECO:0000256|ARBA:ARBA00007975}.
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DR   EMBL; CM022217; KAF7024501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6ELV8; -.
DR   SMR; A0A3B6ELV8; -.
DR   STRING; 4565.A0A3B6ELV8; -.
DR   EnsemblPlants; TraesCS3A02G354200.2; TraesCS3A02G354200.2; TraesCS3A02G354200.
DR   Gramene; TraesCS3A02G354200.2; TraesCS3A02G354200.2; TraesCS3A02G354200.
DR   Gramene; TraesCS3A03G0842900.2; TraesCS3A03G0842900.2.CDS; TraesCS3A03G0842900.
DR   OrthoDB; 367877at2759; -.
DR   Proteomes; UP000019116; Chromosome 3A.
DR   Proteomes; UP000815260; Chromosome 3A.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR000778; Cyt_b245_heavy_chain.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR013623; NADPH_Ox.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   PANTHER; PTHR11972:SF54; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN J-RELATED; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   Pfam; PF08414; NADPH_Ox; 1.
DR   PRINTS; PR00466; GP91PHOX.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        301..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        480..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        669..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..212
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          535..663
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  95749 MW;  E94876E5B3B93D72 CRC64;
     MASPGGGYAD RPAPPLDGMI TVDGGGGRTP PPAGLPRPPG FRGLMQQPSR LASGVRQFAS
     RVSMKVPEVV PGIRPGGGRM TRMQSSAQMG LKGLRFLDKT SGSKEGWKAV ERRFDEMSKA
     SGRLPKESFG KCIGMGDSKE FAGELFVTLS RRRSIEPEQG ITKEQLREFW TEMTDQNFDS
     RLRIFFDMCD KNGDGMLTED EVKEVIILSA SANKLAKLKS HAATYSSLIM EELDPDDRGY
     IEIWQLETLL RGMVSAQAPE VKLKRTTSSL ARTMIPMRYR SPLKRHVTRT MDFVHENWKR
     IWLVTLWLAA NLALFVYKFE QYKHRSSFQV MGNCVCVAKG AAETLKLNMA LILLPVCRNT
     LTTLRSTALS HVIPFDDNIN FHKVLAGAIA VGTVVHTLAH VTCDFPRLVS CPSDKFMALL
     GPNFGFRQPT YPDLLASAPG VTGILMIIIM TFSFTLAMHT FRRSVVKLPS PLHHLAGFNA
     FWYAHHLLLL VYVLLVVHSY FIFLTRVWYK KTTWMFLIVP VLFYACERII RKVRENNYHV
     NILKAAIYPG NVLSLHMKKP PGFKYKSGMY LFVKCPDVSP FEWHPFSITS APGDDYLSVH
     IRTLGDWTSE LRNLFGKCFE AQVTSKKATL SRLETTVVAD SATEDTRFPK VFIDGPYGAP
     AQNYKKYDIL LLIGLGIGAT PFISILKDLL NNIKSNDEVE SIHGSEIGSF KNSGPGRAYF
     YWVTREQGSF DWFKGVMNEV ADNDHSDVIE MHNYLTSVYE EGDARSALIA MVQSLQHAKN
     GVDIVSGSKI RTHFARPNWR KVFSDLANAH KNSRIGVFYC GSPTLTKQLK DLSKEFSQTT
     TTRFHFHKEN F
//
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